Evidence map›Paper›PMID 25797001›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2015

MAS NMR of HIV-1 protein assemblies.

Christopher L Suiter, Caitlin M Quinn, Manman Lu, Guangjin Hou, Huilan Zhang, Tatyana Polenova

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Christopher L SuiterDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA 15261, United States. Electronic address: csuiter@udel.edu.
Caitlin M QuinnDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA 15261, United States. Electronic address: cmquinn@udel.edu.
Manman LuDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA 15261, United States. Electronic address: lumm@udel.edu.
Guangjin HouDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA 15261, United States. Electronic address: hou@udel.edu.
Huilan ZhangDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States. Electronic address: zhang@udel.edu.
Tatyana PolenovaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA 15261, United States. Electronic address: tpolenov@udel.edu.

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
UDE COBRE: STRAINED MOLECULES FOR SYNTHESIS OF UNNATURAL AMINO ACIDSP20RR017716 · NCRR · UNIVERSITY OF DELAWARE · PI BEEBE, THOMAS PAUL · 2002 to 2011
$16.9M
COBRE on Membrane Protein Production and CharacterizationP30GM103519 · NIGMS · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2012 to 2014
$3.3M
MAS NMR Studies of the NIV-1 Gag Polyprotein Assembled into Virus-Like ParticlesF32GM113452 · NIGMS · UNIVERSITY OF DELAWARE · PI QUINN, CAITLIN · 2015 to 2016
$109k
NCRR NIH HHS 5P20RR017716NCRR NIH HHS P20 RR017716NIGMS NIH HHS 5P30GM103519NIGMS NIH HHS F32 GM113452NIGMS NIH HHS P30 GM103519NIGMS NIH HHS P50 GM082251NIGMS NIH HHS P50GM082251
6 · The paper itself

Abstract

The negative global impact of the AIDS pandemic is well known. In this perspective article, the utility of magic angle spinning (MAS) NMR spectroscopy to answer pressing questions related to the structure and dynamics of HIV-1 protein assemblies is examined. In recent years, MAS NMR has undergone major technological developments enabling studies of large viral assemblies. We discuss some of these evolving methods and technologies and provide a perspective on the current state of MAS NMR as applied to the investigations into structure and dynamics of HIV-1 assemblies of CA capsid protein and of Gag maturation intermediates.

Indexed as

Virus AssemblyHIV-1Molecular ImagingNuclear Magnetic Resonance, BiomolecularProtein ConformationViral ProteinsViral ProteinsCACapsid proteinGag polyproteinHIV-1HIV-AIDSMagic angle spinningMASSolid-state NMR

Identifiers

PMID25797001
PMCPMC4432874

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.